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Phenolphthiocerol synthesis polyketide synthase type I Pks15/1 (Beta-ketoacyl-acyl-carrier-protein synthase I) (EC 2.3.1.41)

 MSL7_MYCMM              Reviewed;        2104 AA.
B2HIL7;
05-APR-2011, integrated into UniProtKB/Swiss-Prot.
10-JUN-2008, sequence version 1.
22-NOV-2017, entry version 75.
RecName: Full=Phenolphthiocerol synthesis polyketide synthase type I Pks15/1;
AltName: Full=Beta-ketoacyl-acyl-carrier-protein synthase I;
EC=2.3.1.41;
Name=pks15/1; Synonyms=msl7; OrderedLocusNames=MMAR_1762;
Mycobacterium marinum (strain ATCC BAA-535 / M).
Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
Mycobacterium.
NCBI_TaxID=216594;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC BAA-535 / M;
PubMed=18403782; DOI=10.1101/gr.075069.107;
Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K.,
Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T.,
Churcher C., Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N.,
Jagels K., Lord A., Moule S., Mungall K., Norbertczak H., Quail M.A.,
Rabbinowitsch E., Walker D., White B., Whitehead S., Small P.L.,
Brosch R., Ramakrishnan L., Fischbach M.A., Parkhill J., Cole S.T.;
"Insights from the complete genome sequence of Mycobacterium marinum
on the evolution of Mycobacterium tuberculosis.";
Genome Res. 18:729-741(2008).
[2]
FUNCTION AS A POLYKETIDE SYNTHASE, AND MUTAGENESIS OF CYS-211 AND
SER-2039.
STRAIN=ATCC BAA-535 / M;
PubMed=19799378; DOI=10.1021/ja904792q;
He W., Soll C.E., Chavadi S.S., Zhang G., Warren J.D., Quadri L.E.;
"Cooperation between a coenzyme A-independent stand-alone initiation
module and an iterative type I polyketide synthase during synthesis of
mycobacterial phenolic glycolipids.";
J. Am. Chem. Soc. 131:16744-16750(2009).
-!- FUNCTION: Catalyzes the elongation by iterative transfer of p-
hydroxybenzoyl group from FadD22 (pHBA-S-FAdD22) to form p-
hydroxyphenylalkanoate (pHPA) intermediates during
phenolphthiocerol (PPOL) biosynthesis. PPOL is an important
intermediate in the biosynthesis of phenolic glycolipid (mycosid
B). {ECO:0000269|PubMed:19799378}.
-!- CATALYTIC ACTIVITY: Acyl-[acyl-carrier-protein] + malonyl-[acyl-
carrier-protein] = 3-oxoacyl- [acyl-carrier-protein] + CO(2) +
[acyl-carrier-protein]. {ECO:0000255|PROSITE-ProRule:PRU10022}.
-!- COFACTOR:
Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
Evidence={ECO:0000250};
Note=Binds 1 phosphopantetheine covalently. {ECO:0000250};
-!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
-!- SIMILARITY: Belongs to the beta-ketoacyl-ACP synthases family.
{ECO:0000305}.
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EMBL; CP000854; ACC40211.1; -; Genomic_DNA.
RefSeq; WP_012393570.1; NC_010612.1.
ProteinModelPortal; B2HIL7; -.
SMR; B2HIL7; -.
STRING; 216594.MMAR_1762; -.
EnsemblBacteria; ACC40211; ACC40211; MMAR_1762.
KEGG; mmi:MMAR_1762; -.
eggNOG; ENOG4108JA1; Bacteria.
eggNOG; COG3321; LUCA.
HOGENOM; HOG000046292; -.
KO; K12430; -.
OMA; RLSKEWR; -.
OrthoDB; POG091H06Z6; -.
UniPathway; UPA00094; -.
Proteomes; UP000001190; Chromosome.
GO; GO:0034081; C:polyketide synthase complex; IDA:UniProtKB.
GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:UniProtKB-EC.
GO; GO:0048037; F:cofactor binding; IEA:InterPro.
GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
GO; GO:0071766; P:Actinobacterium-type cell wall biogenesis; IDA:UniProtKB.
GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0008610; P:lipid biosynthetic process; IDA:UniProtKB.
Gene3D; 1.10.1200.10; -; 1.
Gene3D; 3.30.70.250; -; 1.
Gene3D; 3.40.47.10; -; 2.
InterPro; IPR036736; ACP-like_sf.
InterPro; IPR014043; Acyl_transferase.
InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
InterPro; IPR013149; ADH_C.
InterPro; IPR013154; ADH_N.
InterPro; IPR011032; GroES-like_sf.
InterPro; IPR032821; KAsynt_C_assoc.
InterPro; IPR018201; Ketoacyl_synth_AS.
InterPro; IPR014031; Ketoacyl_synth_C.
InterPro; IPR014030; Ketoacyl_synth_N.
InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
InterPro; IPR020801; PKS_acyl_transferase.
InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
InterPro; IPR020807; PKS_dehydratase.
InterPro; IPR020843; PKS_ER.
InterPro; IPR013968; PKS_KR.
InterPro; IPR020806; PKS_PP-bd.
InterPro; IPR015083; Polyketide_synth_docking.
InterPro; IPR036299; Polyketide_synth_docking_sf.
InterPro; IPR009081; PP-bd_ACP.
InterPro; IPR006162; Ppantetheine_attach_site.
InterPro; IPR016039; Thiolase-like.
Pfam; PF00698; Acyl_transf_1; 1.
Pfam; PF08240; ADH_N; 1.
Pfam; PF00107; ADH_zinc_N; 1.
Pfam; PF08990; Docking; 1.
Pfam; PF16197; KAsynt_C_assoc; 1.
Pfam; PF00109; ketoacyl-synt; 1.
Pfam; PF02801; Ketoacyl-synt_C; 1.
Pfam; PF08659; KR; 1.
Pfam; PF00550; PP-binding; 1.
Pfam; PF14765; PS-DH; 1.
SMART; SM00827; PKS_AT; 1.
SMART; SM00826; PKS_DH; 1.
SMART; SM00829; PKS_ER; 1.
SMART; SM00825; PKS_KS; 1.
SMART; SM00823; PKS_PP; 1.
SUPFAM; SSF101173; SSF101173; 1.
SUPFAM; SSF47336; SSF47336; 1.
SUPFAM; SSF50129; SSF50129; 1.
SUPFAM; SSF51735; SSF51735; 3.
SUPFAM; SSF52151; SSF52151; 2.
SUPFAM; SSF53901; SSF53901; 1.
SUPFAM; SSF55048; SSF55048; 1.
PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
PROSITE; PS50075; CARRIER; 1.
PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
1: Evidence at protein level;
Acyltransferase; Complete proteome; Fatty acid metabolism;
Lipid metabolism; Multifunctional enzyme; Phosphopantetheine;
Phosphoprotein; Reference proteome; Transferase.
CHAIN 1 2104 Phenolphthiocerol synthesis polyketide
synthase type I Pks15/1.
/FTId=PRO_0000406361.
DOMAIN 2004 2079 Carrier. {ECO:0000255|PROSITE-
ProRule:PRU00258}.
NP_BIND 1530 1547 NADP. {ECO:0000250}.
NP_BIND 1719 1734 NADP. {ECO:0000250}.
REGION 37 466 Beta-ketoacyl synthase. {ECO:0000250}.
REGION 571 887 Acyltransferase. {ECO:0000250}.
REGION 935 1095 Dehydratase. {ECO:0000250}.
REGION 1400 1705 Enoylreductase. {ECO:0000250}.
REGION 1718 1899 Beta-ketoacyl reductase (KR).
ACT_SITE 211 211 For beta-ketoacyl synthase activity.
{ECO:0000305}.
ACT_SITE 662 662 For acyltransferase activity.
{ECO:0000255|PROSITE-ProRule:PRU10022}.
MOD_RES 2039 2039 O-(pantetheine 4'-phosphoryl)serine.
{ECO:0000255|PROSITE-ProRule:PRU00258}.
MUTAGEN 211 211 C->A: The pHBA starter unit is not loaded
onto Pks15/1 and thus the pHPA
intermediate is not produced.
{ECO:0000269|PubMed:19799378}.
MUTAGEN 2039 2039 S->A: The pHBA starter unit is loaded
onto Pks15/1, but the pHPA intermediate
is not produced.
{ECO:0000269|PubMed:19799378}.
SEQUENCE 2104 AA; 217744 MW; 7A33F823206BDCA5 CRC64;
MTTSGESADQ QNDKLFRYLK KVAVELDEAR ARLREYEQRA TEPVAVVGIG CRFPGGADGP
EGLWDLVSQG RDAVTEFPND RGWDTEGLFD PDPDAEGKTY TRWGAFVENA TNFDAGFFGI
PPSEVLAMDP QQRLMLEVSW EALEHAGIDP MSLRGSSTGV FTGIFAPSYG GKDVGALQGY
GLTGSPVSVA SGRVAYVLGL EGPALSVDTA CSSSLVAIHW AMASLRSGEC DMALAGGVTV
MGLPSIFVGF SRQRGLAADG RCKAFAAAAD GTGWGEGAGV LVLERLSDAQ RNGHNVLAVV
RGSAINQDGA SNGLTAPNGL AQQRVIQAAL ANCGLTSADV DVVEAHGTAT TLGDPIEAEA
LLATYGQGRP TDQPLWVGSI KSNMGHTQAA AGVAGVIKMV QAMRHGLMPA SLHVDEPSKR
VDWESGAVSV LAEARDWPDA GRPRRAGVSS FGISGTNAHV ILEEAPAPEA VPDSESNKGE
PSLPVVPWVI SARSAEALTA QAGRLLAHVQ ADPQSNPVDI GFSLAGRSAF EHRAVVVGAD
RQQLLTGLAT LADGAPGAGV VTGQAGSVGK TAVVFPGQGS QRIGMARELH DQLPVFAEAF
DAVADELDRH LRIPLREVMW GSDAALLDST EFAQPALFAV EVALFAALQR WGLQPDFVMG
HSVGELSAAY VAGVLTLADA AMLVVARGRL MQALPAGGAM VAVAAAEDEV LPSLTDGVGI
AAINAPKSVV ISGAEAAVTA ISDQFAQQGR RVHRLAVSHA FHSPLMEPML EEFARIAAQV
EAREPQIALV SNVTGELASA DGGFGSAQYW VEHVRRAVRF ADSARQLHTL GVTHFVEVGP
GSGLTGSIEQ SLAPAEAVVV SMLGKDRPEV ASVLTAFGQL FSTGMSVDWP AVFAGSGATR
VDLPTYAFQR RRFWEVPGAD GPADATGLGL GGAEHALLGA VVERPDSGGV VLTGRLALAD
QPWLADHVIG GVVLFPGAGF VELAIRAGDE VGCAVVEELV LAAPLVLHPG MGVQVQVIVG
AADDSGNRAL SVYSRGDQSE DWLLNAEGML GVEAASSGAD LSVWPPEGAE SVDISDGYAQ
LADRGYAYGP GFQGLVGVWR RDSELFAEVV APSGVAVDKM GMHPVVLDAV LHALGLTAEQ
NPDSDETKLP FCWRGVSLHA GGAGRVRARL TMSGPDSISV EIADAAGLPV LTVGALVTRA
MSAAQLRAAV AAAGGGAPDQ GPLDVIWSPI PLSGSGTNGS AQPAVVSWAD FCAGGDGGAA
GDAGVVVWEP NPAGEDVVGS VYAATHAALE VLQSWFDGDR AGTLVVLTHG AVAMPGENVS
DLAGAAVWGI VRSAQAENPG RIVLVDADAA VEAAELVAVG EPQLVVRSGA AHAARLAPAA
PLLAVPADES AWRLAAGGGG TLEDLVIEPC PEVQAPLAAG QVRVAVRAVG VNFRDVVAAL
GMYPGEAPPL GAEGAGVVLE VGPQVSGVAV GDSVMGFLGG AGPLSVVDQQ LITRMPQGWS
FAQAAAVPVV FLTALFGLQD LAKIQPGESV LIHAGTGGVG MAAVQLARHW GVEIFVTASR
GKWDTLRAMG FDDDHIGDSR TLDFEEKFLA VTDGRGVDVV LDSLAGDFVD ASLRLLVRGG
RFLEMGKTDI RDADKIAANY PGVWYRAFDL SEAGPVRMQE MLAEVRELFD TAVLHRLPVT
TWDVRCAPAA FRFMSQARHI GKVVLTMPSA LADGLADATV LITGATGAVG AVLARHMLDA
YGVRHLVLAS RRGDRAEGAA ELAAELSEAG ANVQVVACDV ADRDAVEAML ARLSGEYPPV
RGVIHAAGVL DDAVISSLTP ERIDTVLRAK VDAAWNLHEA TLDLDLSMFV LCSSIAATVG
SPGQGNYSAA NSFLDGLAAH RQAAGLAGIS VAWGLWEQSG GMAAHLSSRD LARMSRSGLA
PMNPEQAVGL LDAVLAINHP LMVATLLDRP ALEARAQAGG LPPLFAGVVR RPRRRQIEDT
GDAAQSKSAL AERLNGLSAG ERQDALVGLV CLQAAAVLGR PSPEDIDPEA GFQDLGFDSL
TAVELRNRLK SATGLTLPPT VIFDHPTPTA IAEYVGRQIP DSQATQAEEE KLPESDGEMV
SVTA


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